Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
29
|
| pubmed:dateCreated |
1989-11-17
|
| pubmed:abstractText |
It has been claimed that the inositol 1,4,5-trisphosphate-sensitive calcium pool in liver and pancreatic acinar cells is located in specified organelles ("calciosomes") which are characterized by their content of the calcium-binding protein calsequestrin (Volpe, P., Krause, K. H., Hashimoto, S., Zorzato, F., Pozzan, T., Meldolesi, J., and Lew, D. P. (1988) Proc. Natl. Acad. Sci. U. S. A. 85, 1091-1095). We show here that the inositol 1,4,5-trisphosphate-sensitive compartment of rat liver does not contain calsequestrin-like material. Instead four non-membraneous calcium-binding glycoproteins with approximate molecular masses of 59, 60, 80, and 90 kDa were found. The 59-, 80-, and 90-kDa proteins were of the high mannose-rich type, the carbohydrate moiety of the 60-kDa protein was of the complex hybrid type with terminal galactoses. All four proteins had high affinity binding sites for calcium (KD between 1 and 5 microM) and from 1 to 5 binding sites/molecule. The 80- and the 90-kDa proteins had also low affinity binding sites (KD 400 and 600 microM, respectively, with 13 and 15 binding sites/molecule, respectively). A comparison of the NH2-terminal sequences revealed that the 60-kDa calcium-binding protein represents the rat liver calregulin, whereas the 90-kDa calcium-binding protein represents grp94. The sequences did not reveal any relationship of the 80-kDa protein with grp78, or of the 59-kDa protein with protein disulfide isomerase.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calreticulin,
http://linkedlifedata.com/resource/pubmed/chemical/Calsequestrin,
http://linkedlifedata.com/resource/pubmed/chemical/Galactose,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol 1,4,5-Trisphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Mannose,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
264
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
17494-501
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:2793869-Amino Acid Sequence,
pubmed-meshheading:2793869-Animals,
pubmed-meshheading:2793869-Binding Sites,
pubmed-meshheading:2793869-Calcium,
pubmed-meshheading:2793869-Calcium-Binding Proteins,
pubmed-meshheading:2793869-Calreticulin,
pubmed-meshheading:2793869-Calsequestrin,
pubmed-meshheading:2793869-Endoplasmic Reticulum,
pubmed-meshheading:2793869-Galactose,
pubmed-meshheading:2793869-Glycoproteins,
pubmed-meshheading:2793869-Inositol 1,4,5-Trisphosphate,
pubmed-meshheading:2793869-Male,
pubmed-meshheading:2793869-Mannose,
pubmed-meshheading:2793869-Microsomes, Liver,
pubmed-meshheading:2793869-Molecular Sequence Data,
pubmed-meshheading:2793869-Molecular Weight,
pubmed-meshheading:2793869-Muscles,
pubmed-meshheading:2793869-Phosphorylation,
pubmed-meshheading:2793869-Rats,
pubmed-meshheading:2793869-Rats, Inbred Strains,
pubmed-meshheading:2793869-Ribonucleoproteins
|
| pubmed:year |
1989
|
| pubmed:articleTitle |
Four intracisternal calcium-binding glycoproteins from rat liver microsomes with high affinity for calcium. No indication for calsequestrin-like proteins in inositol 1,4,5-trisphosphate-sensitive calcium sequestering rat liver vesicles.
|
| pubmed:affiliation |
Zentrum Innere Medizin, Universität Göttingen, Federal Republic of Germany.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|